BMRB Entry 19126
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19126
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Title: Structure of full-length transmembrane domains of human glycine receptor 1 monomer subunit PubMed: 23994010
Deposition date: 2013-03-28 Original release date: 2013-09-03
Authors: Mowrey, David; Cui, Tanxing; Jia, Yuanyuan; Ma, Dejian; Makhov, Alexander; Zhang, Peijun; Tang, Pei; Xu, Yan
Citation: Mowrey, David; Cui, Tanxing; Jia, Yuanyuan; Ma, Dejian; Makhov, Alexander; Zhang, Peijun; Tang, Pei; Xu, Yan. "Open-Channel Structures of the Human Glycine Receptor 1 Full-Length Transmembrane Domain." Structure 21, 1897-1904 (2013).
Assembly members:
GlyR, polymer, 150 residues, 17320.490 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
GlyR: MLERQLGYYLIQLYIPSLLI
VILSWISFWINLDAAPARVG
LGITTVLTLTTQSSGSRASL
PKVSYVKAIDIWLAVCLLFV
FSALLEYAAVNFVSRQREFG
GGGFIQRAKKIDKISRIGFP
LAFLIFNLFYWIIYKIVRRE
DEFEHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 283 |
15N chemical shifts | 155 |
1H chemical shifts | 707 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | GlyR | 1 |
Entities:
Entity 1, GlyR 150 residues - 17320.490 Da.
1 | MET | LEU | GLU | ARG | GLN | LEU | GLY | TYR | TYR | LEU | |
2 | ILE | GLN | LEU | TYR | ILE | PRO | SER | LEU | LEU | ILE | |
3 | VAL | ILE | LEU | SER | TRP | ILE | SER | PHE | TRP | ILE | |
4 | ASN | LEU | ASP | ALA | ALA | PRO | ALA | ARG | VAL | GLY | |
5 | LEU | GLY | ILE | THR | THR | VAL | LEU | THR | LEU | THR | |
6 | THR | GLN | SER | SER | GLY | SER | ARG | ALA | SER | LEU | |
7 | PRO | LYS | VAL | SER | TYR | VAL | LYS | ALA | ILE | ASP | |
8 | ILE | TRP | LEU | ALA | VAL | CYS | LEU | LEU | PHE | VAL | |
9 | PHE | SER | ALA | LEU | LEU | GLU | TYR | ALA | ALA | VAL | |
10 | ASN | PHE | VAL | SER | ARG | GLN | ARG | GLU | PHE | GLY | |
11 | GLY | GLY | GLY | PHE | ILE | GLN | ARG | ALA | LYS | LYS | |
12 | ILE | ASP | LYS | ILE | SER | ARG | ILE | GLY | PHE | PRO | |
13 | LEU | ALA | PHE | LEU | ILE | PHE | ASN | LEU | PHE | TYR | |
14 | TRP | ILE | ILE | TYR | LYS | ILE | VAL | ARG | ARG | GLU | |
15 | ASP | GLU | PHE | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: GlyR 480 uM; H2O 95%; D2O 5%
sample_2: GlyR 480 uM; H2O 95%; D2O 5%
sample_3: GlyR 480 uM; H2O 95%; D2O 5%
sample_4: GlyR 480 uM; H2O 95%; D2O 5%
sample_5: GlyR 480 uM; H2O 95%; D2O 5%
sample_6: GlyR 480 uM; H2O 95%; D2O 5%
sample_7: GlyR 480 uM; H2O 95%; D2O 5%
sample_conditions_1: pH: 5.8; pressure: 1 atm; temperature: 313 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0 -
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz
- Bruker Avance 900 MHz
Related Database Links:
PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts